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P10795

- RBS1A_ARATH

UniProt

P10795 - RBS1A_ARATH

Protein

Ribulose bisphosphate carboxylase small chain 1A, chloroplastic

Gene

RBCS-1A

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 140 (01 Oct 2014)
      Sequence version 2 (10 Jan 2003)
      Previous versions | rss
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    Functioni

    RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate. Both reactions occur simultaneously and in competition at the same active site By similarity.By similarity

    Catalytic activityi

    2 3-phospho-D-glycerate + 2 H+ = D-ribulose 1,5-bisphosphate + CO2 + H2O.
    3-phospho-D-glycerate + 2-phosphoglycolate = D-ribulose 1,5-bisphosphate + O2.

    GO - Molecular functioni

    1. copper ion binding Source: TAIR
    2. monooxygenase activity Source: UniProtKB-KW
    3. ribulose-bisphosphate carboxylase activity Source: UniProtKB-EC

    GO - Biological processi

    1. chloroplast ribulose bisphosphate carboxylase complex biogenesis Source: TAIR
    2. photorespiration Source: UniProtKB-KW
    3. photosynthesis Source: TAIR
    4. reductive pentose-phosphate cycle Source: UniProtKB-KW
    5. response to blue light Source: TAIR
    6. response to cold Source: TAIR
    7. response to far red light Source: TAIR
    8. response to red light Source: TAIR

    Keywords - Molecular functioni

    Lyase, Monooxygenase, Oxidoreductase

    Keywords - Biological processi

    Calvin cycle, Carbon dioxide fixation, Photorespiration, Photosynthesis

    Enzyme and pathway databases

    BioCyciARA:GQT-1261-MONOMER.
    MetaCyc:AT1G67090-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ribulose bisphosphate carboxylase small chain 1A, chloroplastic (EC:4.1.1.39)
    Short name:
    RuBisCO small subunit 1A
    Gene namesi
    Name:RBCS-1A
    Synonyms:ATS1A
    Ordered Locus Names:At1g67090
    ORF Names:F1O19.14, F5A8.1
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 1

    Organism-specific databases

    TAIRiAT1G67090.

    Subcellular locationi

    Plastidchloroplast membrane 1 Publication; Peripheral membrane protein 1 Publication. Plastidchloroplast stroma 1 Publication

    GO - Cellular componenti

    1. apoplast Source: TAIR
    2. chloroplast Source: TAIR
    3. chloroplast envelope Source: TAIR
    4. chloroplast membrane Source: UniProtKB-SubCell
    5. chloroplast stroma Source: TAIR
    6. chloroplast thylakoid membrane Source: TAIR
    7. cytosolic ribosome Source: TAIR
    8. membrane Source: TAIR
    9. thylakoid Source: TAIR
    10. thylakoid lumen Source: TAIR

    Keywords - Cellular componenti

    Chloroplast, Membrane, Plastid

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 5555ChloroplastAdd
    BLAST
    Chaini56 – 180125Ribulose bisphosphate carboxylase small chain 1A, chloroplasticPRO_0000031463Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei113 – 1131Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiP10795.
    PRIDEiP10795.

    2D gel databases

    World-2DPAGE0003:P10795.

    Expressioni

    Gene expression databases

    GenevestigatoriP10795.

    Interactioni

    Subunit structurei

    8 large chains + 8 small chains.

    Protein-protein interaction databases

    BioGridi28250. 5 interactions.
    IntActiP10795. 6 interactions.
    MINTiMINT-2584041.

    Structurei

    3D structure databases

    ProteinModelPortaliP10795.
    SMRiP10795. Positions 56-178.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the RuBisCO small chain family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG4451.
    HOGENOMiHOG000141332.
    InParanoidiP10795.
    KOiK01602.
    OMAiAFPATRK.
    PhylomeDBiP10795.

    Family and domain databases

    Gene3Di3.30.190.10. 1 hit.
    InterProiIPR024681. RuBisCO_sc.
    IPR000894. RuBisCO_sc_dom.
    IPR024680. RuBisCO_ssu_N.
    [Graphical view]
    PfamiPF12338. RbcS. 1 hit.
    PF00101. RuBisCO_small. 1 hit.
    [Graphical view]
    PRINTSiPR00152. RUBISCOSMALL.
    SMARTiSM00961. RuBisCO_small. 1 hit.
    [Graphical view]
    SUPFAMiSSF55239. SSF55239. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 1 isoform i produced by alternative splicing. Align

    Note: A number of isoforms are produced. According to EST sequences.

    Isoform 1 (identifier: P10795-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

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    MASSMLSSAT MVASPAQATM VAPFNGLKSS AAFPATRKAN NDITSITSNG    50
    GRVNCMQVWP PIGKKKFETL SYLPDLTDSE LAKEVDYLIR NKWIPCVEFE 100
    LEHGFVYREH GNSPGYYDGR YWTMWKLPLF GCTDSAQVLK EVEECKKEYP 150
    NAFIRIIGFD NTRQVQCISF IAYKPPSFTG 180
    Length:180
    Mass (Da):20,216
    Last modified:January 10, 2003 - v2
    Checksum:i5DE768676D61F8F7
    GO

    Sequence cautioni

    The sequence AAK49590.1 differs from that shown. Reason: Erroneous initiation.
    The sequence CAA31948.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti115 – 1151G → R in AAG40356. (PubMed:14593172)Curated
    Sequence conflicti171 – 1711I → V in CAA31948. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X13611 Genomic DNA. Translation: CAA31948.1. Sequence problems.
    AC004146 Genomic DNA. Translation: AAD10655.1.
    AC007152 Genomic DNA. No translation available.
    CP002684 Genomic DNA. Translation: AEE34594.1.
    AF325011 mRNA. Translation: AAG40363.1.
    AF325004 mRNA. Translation: AAG40356.1.
    AF372874 mRNA. Translation: AAK49590.1. Different initiation.
    AF410291 mRNA. Translation: AAK95277.1.
    AY054188 mRNA. Translation: AAL06849.1.
    AY054581 mRNA. Translation: AAK96772.1.
    AY058831 mRNA. Translation: AAL24219.1.
    AY059940 mRNA. Translation: AAL24422.1.
    AY062612 mRNA. Translation: AAL32690.1.
    AY062711 mRNA. Translation: AAL32789.1.
    AY065101 mRNA. Translation: AAL38277.1.
    AY093380 mRNA. Translation: AAM13379.1.
    AY093388 mRNA. Translation: AAM13387.1.
    AY097366 mRNA. Translation: AAM19882.1.
    BT000362 mRNA. Translation: AAN15681.1.
    BT002076 mRNA. Translation: AAN72087.1.
    X68342 Other DNA. Translation: CAA48415.1. Different termination.
    PIRiG96694.
    S03720. RKMUA1.
    RefSeqiNP_176880.1. NM_105379.3. [P10795-1]
    UniGeneiAt.12721.
    At.30194.
    At.37531.
    At.46639.
    At.49098.
    At.67454.
    At.68122.
    At.70032.
    At.70053.

    Genome annotation databases

    EnsemblPlantsiAT1G67090.1; AT1G67090.1; AT1G67090. [P10795-1]
    GeneIDi843029.
    KEGGiath:AT1G67090.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X13611 Genomic DNA. Translation: CAA31948.1 . Sequence problems.
    AC004146 Genomic DNA. Translation: AAD10655.1 .
    AC007152 Genomic DNA. No translation available.
    CP002684 Genomic DNA. Translation: AEE34594.1 .
    AF325011 mRNA. Translation: AAG40363.1 .
    AF325004 mRNA. Translation: AAG40356.1 .
    AF372874 mRNA. Translation: AAK49590.1 . Different initiation.
    AF410291 mRNA. Translation: AAK95277.1 .
    AY054188 mRNA. Translation: AAL06849.1 .
    AY054581 mRNA. Translation: AAK96772.1 .
    AY058831 mRNA. Translation: AAL24219.1 .
    AY059940 mRNA. Translation: AAL24422.1 .
    AY062612 mRNA. Translation: AAL32690.1 .
    AY062711 mRNA. Translation: AAL32789.1 .
    AY065101 mRNA. Translation: AAL38277.1 .
    AY093380 mRNA. Translation: AAM13379.1 .
    AY093388 mRNA. Translation: AAM13387.1 .
    AY097366 mRNA. Translation: AAM19882.1 .
    BT000362 mRNA. Translation: AAN15681.1 .
    BT002076 mRNA. Translation: AAN72087.1 .
    X68342 Other DNA. Translation: CAA48415.1 . Different termination.
    PIRi G96694.
    S03720. RKMUA1.
    RefSeqi NP_176880.1. NM_105379.3. [P10795-1 ]
    UniGenei At.12721.
    At.30194.
    At.37531.
    At.46639.
    At.49098.
    At.67454.
    At.68122.
    At.70032.
    At.70053.

    3D structure databases

    ProteinModelPortali P10795.
    SMRi P10795. Positions 56-178.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 28250. 5 interactions.
    IntActi P10795. 6 interactions.
    MINTi MINT-2584041.

    2D gel databases

    World-2DPAGE 0003:P10795.

    Proteomic databases

    PaxDbi P10795.
    PRIDEi P10795.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT1G67090.1 ; AT1G67090.1 ; AT1G67090 . [P10795-1 ]
    GeneIDi 843029.
    KEGGi ath:AT1G67090.

    Organism-specific databases

    TAIRi AT1G67090.

    Phylogenomic databases

    eggNOGi COG4451.
    HOGENOMi HOG000141332.
    InParanoidi P10795.
    KOi K01602.
    OMAi AFPATRK.
    PhylomeDBi P10795.

    Enzyme and pathway databases

    BioCyci ARA:GQT-1261-MONOMER.
    MetaCyc:AT1G67090-MONOMER.

    Gene expression databases

    Genevestigatori P10795.

    Family and domain databases

    Gene3Di 3.30.190.10. 1 hit.
    InterProi IPR024681. RuBisCO_sc.
    IPR000894. RuBisCO_sc_dom.
    IPR024680. RuBisCO_ssu_N.
    [Graphical view ]
    Pfami PF12338. RbcS. 1 hit.
    PF00101. RuBisCO_small. 1 hit.
    [Graphical view ]
    PRINTSi PR00152. RUBISCOSMALL.
    SMARTi SM00961. RuBisCO_small. 1 hit.
    [Graphical view ]
    SUPFAMi SSF55239. SSF55239. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Four genes in two diverged subfamilies encode the ribulose-1,5-bisphosphate carboxylase small subunit polypeptides of Arabidopsis thaliana."
      Krebbers E., Seurinck J., Herdies L., Cashmore A.R., Timko M.P.
      Plant Mol. Biol. 11:745-759(1988)
      [AGRICOLA] [Europe PMC]
      Cited for: NUCLEOTIDE SEQUENCE.
      Strain: cv. Columbia K85.
    2. "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
      Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K.
      , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
      Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    3. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    4. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
      Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
      , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
      Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: cv. Columbia.
    5. "Arabidopsis thaliana small subunit leader and transit peptide enhance the expression of Bacillus thuringiensis proteins in transgenic plants."
      Wong E.Y., Hironaka C.M., Fishhoff D.A.
      Plant Mol. Biol. 20:81-93(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE OF 1-79.
    6. "Proteomics of the chloroplast envelope membranes from Arabidopsis thaliana."
      Ferro M., Salvi D., Brugiere S., Miras S., Kowalski S., Louwagie M., Garin J., Joyard J., Rolland N.
      Mol. Cell. Proteomics 2:325-345(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
      Strain: cv. Wassilewskija.
    7. "Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks."
      Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., Grossmann J., Gruissem W., Baginsky S.
      Plant Physiol. 150:889-903(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiRBS1A_ARATH
    AccessioniPrimary (citable) accession number: P10795
    Secondary accession number(s): Q94JW2, Q9FPI6, Q9SAV4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: January 10, 2003
    Last modified: October 1, 2014
    This is version 140 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    There are four genes coding for RBS in Arabidopsis thaliana.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3